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Receptor Information

>4yf9 Chain L (length=575) Species: 1268622 (Acidovorax sp. MR-S7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SNMYGFGTAATGEGSGVLFGNPHWYWKGPDRFYQAQLTIDGEANVSGVSF
LGLPVIQIGFNDSVAWSHTVSTARRFGFFQLSLVQGEPTSYLRDGVPVKM
KPATITVPSRNADGSVSDVTRTLYHSEFGPLVNLAGLNPALAWSQGTAFA
IRDINGENFRTLRTWMRWNQAKSLDEFIAIQKEEASIPWVNTVAVGRGSA
KAWYADIGAVPNVSPAQTAACTTPFGMAVGQALPNVPFFDGSRSECDWLT
DADSVQKGAVGVSRMPSLQRDDYVGNMNDSYWLANVHAPLTGYPAIFGPA
GTSAQTLRTRMGHTMALERLAGTDGYAGNKATSAVVREMVLGSRVFSAER
FKDEVLDLICTPAQWTVNGAAVDAAQACAVLAAWDNRGRKDSRGSHLWDE
FWSRVPTASLFTVPFSAADPLNTPRGINAAAADALRQAMATAIARVGQSG
YALDAPRGEVLYATRGGTRLPLYGGCGAMGYFTITCSENDITQGGYSMDG
QPNASNSYMQVVSFPASGVQAHTFLTFSLSDDPASPHHGDYTKAYSAGQW
LRVPFTEAEITGNADYRTATVKELE

>4yf9 Chain K (length=16) Species: 1268622 (Acidovorax sp. MR-S7) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

FEPGRTRAPSLQVGGE

Receptor-Ligand Complex Structure

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Structure summary

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PDB	4yf9 Bifunctional quorum-quenching and antibiotic-acylase MacQ forms a 170-kDa capsule-shaped molecule containing spacer polypeptides
Resolution	2.6 Å
Binding residue (original residue number in PDB)	V70 R74 L137 N138 A228 L233
Binding residue (residue number reindexed from 1)	V70 R74 L137 N138 A228 L233

Catalytic site (original residue number in PDB)	S1 H23 V70 N278 N506
Catalytic site (residue number reindexed from 1)	S1 H23 V70 N278 N506
Enzyme Commision number	?

	Molecular Function
GO:0016787	hydrolase activity

	Biological Process
GO:0017000	antibiotic biosynthetic process

PDB	RCSB:4yf9, PDBe:4yf9, PDBj:4yf9
PDBsum	4yf9
PubMed	28827579
UniProt	A0A0A1VBK6

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Structure of PDB 4yf9 Chain L Binding Site BS01